eF-site ID 4uir-B PDB Code 4uir Chain B click to enlarge Title Structure of oleate hydratase from Elizabethkingia meningoseptica Classification LYASE Compound OLEATE HYDRATASE Source Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) (OLHYD_ELIME) Sequence B:  NPITSKFDKVLNASSEYGHVNHEPDSSKEQQRNTPQKSMP FSDQIGNYQRNKGIPVQSYDNSKIYIIGSGIAGMSAAYYF IRDGHVPAKNITFLEQLHIDGGSLDGAGNPTDGYIIREMD MTYENLWDMFQDIPALEMPAPYSVLDEYRLINDNDSNYSK ARLINNKGEIKDFSKFGLNKMDQLAIIRLLLKNKEELDDL TIEDYFSESFLKSNFWTFWRTMFAFENWHSLLELKLYMHR FLHAIDGLNDLSSLVFPKYNQYDTFVTPLRKFLQEKGVNI HLNTLVKDLDIHINTEGKVVEGIITEQDGKEVKIPVGKND YVIVTTGSMTEDTFYGNNKTAPIIGIDNSTSGQSAGWKLW KNLAAKSEIFGKPEKFCSNIEKSAWESATLTCKPSALIDK LKEYSVNDPYSGKTVTGGIITITDSNWLMSFTCNRQPHFP EQPDDVLVLWVYALFMDKEGNYIKKTMLECTGDEILAELC YHLGIEDQLENVQKNTIVRTAFMPYITSMFMPRAKGDRPR VVPEGCKNLGLVGQFVETNNDVVFTMESSVRTARIAVYKL LNLNKQVPDINPLQYDIRHLLKAAKTLNDDKPFVGEGLLR KVLKGTYFEHVLPAGAAEEESFIAEHVNKFREWV Description Functional site 1) chain B residue 599 type sequence G description BINDING SITE FOR RESIDUE PO4 B 1642 source : AC2 2) chain B residue 600 type sequence E description BINDING SITE FOR RESIDUE PO4 B 1642 source : AC2 3) chain B residue 601 type sequence G description BINDING SITE FOR RESIDUE PO4 B 1642 source : AC2 4) chain B residue 602 type sequence L description BINDING SITE FOR RESIDUE PO4 B 1642 source : AC2 5) chain B residue 250 type sequence D description BINDING SITE FOR RESIDUE NA B 1643 source : AC4 6) chain B residue 253 type sequence N description BINDING SITE FOR RESIDUE NA B 1643 source : AC4 7) chain B residue 122 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:26077980 source Swiss-Prot : SWS_FT_FI1 8) chain B residue 241 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:26077980 source Swiss-Prot : SWS_FT_FI2 9) chain B residue 73 type BINDING sequence A description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 10) chain B residue 96 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 11) chain B residue 97 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 12) chain B residue 104 type BINDING sequence S description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 13) chain B residue 122 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 14) chain B residue 127 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 15) chain B residue 290 type BINDING sequence V description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 16) chain B residue 332 type BINDING sequence S description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 17) chain B residue 549 type BINDING sequence T description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 18) chain B residue 553 type BINDING sequence S description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3

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